ID RASA3_RAT Reviewed; 834 AA.
AC Q9QYJ2; Q09YN9;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 24-JAN-2024, entry version 127.
DE RecName: Full=Ras GTPase-activating protein 3;
DE AltName: Full=GAP1(IP4BP);
DE AltName: Full=Ins P4-binding protein;
DE AltName: Full=R-ras GAP;
GN Name=Rasa3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Iwashita S., Kubo Y., Sezaki M., Hinohara Y., Kobayashi M., Satoh S.,
RA Fukuda M., Nakamura K., Suzuki-Migishima R., Yokoyama M., Ohba M.,
RA Katoh C., Adachi E., Song S.Y.;
RT "Essential role of R-ras GAP in embryogenesis: embryonic lethality by
RT underdeveloped adherent junctions between capillary endothelial cells.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 711-834.
RA Sezaki M., Iwashita S.;
RT "Expression of the R-ras GTPase activating protein gene during rat brain
RT development.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809 AND SER-833, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds
CC inositol tetrakisphosphate (IP4) (By similarity). {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D86045; BAF31891.1; -; mRNA.
DR EMBL; AB028626; BAA89032.1; -; mRNA.
DR RefSeq; NP_113762.1; NM_031574.1.
DR AlphaFoldDB; Q9QYJ2; -.
DR SMR; Q9QYJ2; -.
DR BioGRID; 248025; 2.
DR STRING; 10116.ENSRNOP00000069783; -.
DR iPTMnet; Q9QYJ2; -.
DR PhosphoSitePlus; Q9QYJ2; -.
DR PaxDb; 10116-ENSRNOP00000061587; -.
DR GeneID; 29372; -.
DR KEGG; rno:29372; -.
DR AGR; RGD:69365; -.
DR CTD; 22821; -.
DR RGD; 69365; Rasa3.
DR eggNOG; KOG2059; Eukaryota.
DR InParanoid; Q9QYJ2; -.
DR OrthoDB; 24454at2759; -.
DR PhylomeDB; Q9QYJ2; -.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR PRO; PR:Q9QYJ2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0015278; F:calcium-release channel activity; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR CDD; cd08401; C2A_RasA2_RasA3; 1.
DR CDD; cd04010; C2B_RasA3; 1.
DR CDD; cd13371; PH_GAP1_mammal-like; 1.
DR CDD; cd05134; RasGAP_RASA3; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR037774; RASA3_PH.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001562; Znf_Btk_motif.
DR PANTHER; PTHR10194:SF53; RAS GTPASE-ACTIVATING PROTEIN 3; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00107; BTK; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 1: Evidence at protein level;
KW Acetylation; GTPase activation; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14644"
FT CHAIN 2..834
FT /note="Ras GTPase-activating protein 3"
FT /id="PRO_0000056644"
FT DOMAIN 1..112
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 123..263
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 330..524
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 576..677
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 679..715
FT /note="Btk-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 698
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 699
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 709
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14644"
FT MOD_RES 66
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60790"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60790"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14644"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 778
FT /note="R -> K (in Ref. 2; BAA89032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 834 AA; 96020 MW; 04F9B79A3C2F946F CRC64;
MAVEEEGLRV FQSVRIKIGE AKNLPSYPGP NKMRDCYCTV NLDQEEVFRT KIVEKSLCPF
YGEDFYCEIP RSFRHLSFYI FDRDVFRRDS IIGKVAIQKE DLQRYHNRDT WFQLQHVDAD
SEVQGKVHLE LRLSEVITDT GVVCHKLAAR IFECQGLPIV NGQCDPYATV TLAGPFRSEA
KKTKVKKKTN NPQFDEVFYF EVTRPCSYSK KSHFDFEEED VDKLEIRVDL WNASNLKFGD
EFLGELRIPL HVLRYASSYE AWYFLQPRDN GSKSVKPDDL GSLRLNVVYT EDHVFSSEYY
SPLRDLLLKS ADVEPVSASA AHILGEVCRD KQEAAIPLVR LLLHYGRVVP FISAIASAEV
KRTQDPNTIF RGNSLTSKCI DETMKLAGMH YLHVTLKPTI EEICQSHKSC EIDPVKLKDG
ENLENNMESL RQYVDRIFSV ITKSGVSCPT VMCDIFFSLR EAAAKRFQDD LDVRYTAVSS
FIFLRFFAPA ILSPNLFQLT PHHTDPQTSR TLTLISKTIQ TLGSLSKSKS ASFKESYMAT
FYEFFNEQKY ADAVKNFLDL ISSSGRRDPK SIEQPILLKE GFMIKRAQGR KRFGMKNFKK
RWFRLTNHEF TYQKSKGDQP LCNIPIENIL AVERLEEESF RMKNMFQVIQ PERALYIQAN
NCVEAKDWID ILTKVSQCNQ KRLTVFHPSA YLNGHWLCCR ASSDTAIGCT PCTGGLPANI
QLDIDGDRET ERIYSLFNLY MGKLEKMQEA CGSKSVYDGP EQEEYSTFII DDPQETYRTL
KQVIAGVGTL EQEHAQYRRN KFKKTRYGSQ EHPIGDKSFQ NYIRQQSEIS THSI
//
